Structure of PDB 4f64 Chain A

Receptor sequence
>4f64A (length=278) Species: 9606 (Homo sapiens) [Search protein sequence]
ELPEDPRWELPRDRLVLGKPLGQVVLAEAIGLPNRVTKVAVKMLKSDATE
KDLSDLISEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREY
LQARRPPEEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVTED
NVMKIADFGLARDIHHIDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVW
SFGVLLWEIFTLGGSPYPGVPVEELFKLLKEGHRMDKPSNCTNELYMMMR
DCWHAVPSQRPTFKQLVEDLDRIVALTS
3D structure
PDB4f64 Protein-Ligand Crystal Structures Can Guide the Design of Selective Inhibitors of the FGFR Tyrosine Kinase.
ChainA
Resolution2.05 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D623 A625 R627 N628 D641
Catalytic site (residue number reindexed from 1) D139 A141 R143 N144 D157
Enzyme Commision number 2.7.10.1: receptor protein-tyrosine kinase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 0S8 A L484 A512 V561 A564 S565 G567 L630 L21 A40 V89 A92 S93 G95 L146 MOAD: ic50=63nM
PDBbind-CN: -logKd/Ki=7.20,IC50=63.1nM
BindingDB: IC50=794.33nM
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004713 protein tyrosine kinase activity
GO:0005007 fibroblast growth factor receptor activity
GO:0005524 ATP binding
Biological Process
GO:0006468 protein phosphorylation

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Molecular Function
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Biological Process
External links
PDB RCSB:4f64, PDBe:4f64, PDBj:4f64
PDBsum4f64
PubMed22612866
UniProtP11362|FGFR1_HUMAN Fibroblast growth factor receptor 1 (Gene Name=FGFR1)

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